SCO2_BOVIN
ID SCO2_BOVIN Reviewed; 266 AA.
AC A6H784;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein SCO2 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=SCO2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Copper metallochaperone essential for the synthesis and
CC maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved
CC in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a
CC thiol-disulfide oxidoreductase to regulate the redox state of the
CC cysteines in SCO1 during maturation of MT-CO2/COX2.
CC {ECO:0000250|UniProtKB:O43819}.
CC -!- SUBUNIT: Homodimer. Interacts with COA6. Found in a complex with
CC TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO1. Interacts with
CC TMEM177 in a COX20-dependent manner. Interacts with COX20 in a MT-
CC CO2/COX2- and COX18-dependent manner. Interacts with COX16.
CC {ECO:0000250|UniProtKB:O43819}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O43819}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; BC146150; AAI46151.1; -; mRNA.
DR RefSeq; NP_001098963.1; NM_001105493.2.
DR RefSeq; XP_010804121.1; XM_010805819.2.
DR RefSeq; XP_010804122.1; XM_010805820.2.
DR AlphaFoldDB; A6H784; -.
DR SMR; A6H784; -.
DR STRING; 9913.ENSBTAP00000016742; -.
DR PaxDb; A6H784; -.
DR PRIDE; A6H784; -.
DR Ensembl; ENSBTAT00000016742; ENSBTAP00000016742; ENSBTAG00000012609.
DR GeneID; 100125923; -.
DR KEGG; bta:100125923; -.
DR CTD; 9997; -.
DR VEuPathDB; HostDB:ENSBTAG00000012609; -.
DR VGNC; VGNC:106917; SCO2.
DR eggNOG; KOG2792; Eukaryota.
DR GeneTree; ENSGT00390000004323; -.
DR HOGENOM; CLU_050131_0_3_1; -.
DR InParanoid; A6H784; -.
DR OMA; KHAGRDY; -.
DR OrthoDB; 1462537at2759; -.
DR TreeFam; TF313752; -.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012609; Expressed in olfactory segment of nasal mucosa and 108 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0016531; F:copper chaperone activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:InterPro.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR GO; GO:0003012; P:muscle system process; IEA:Ensembl.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR017276; Synth_of_cyt-c-oxidase_Sco1/2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR PIRSF; PIRSF037736; SCO1; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Copper; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..266
FT /note="Protein SCO2 homolog, mitochondrial"
FT /id="PRO_0000354067"
FT TOPO_DOM 42..60
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..266
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DOMAIN 85..259
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 133
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:O43819"
FT DISULFID 133..137
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 266 AA; 29789 MW; D8CE2DBC2FAECB0F CRC64;
MLLLARPPKA WHRLFQLQPL ALLGTPGGKT QHVRYQLFST PGPADTGRQG QPQGPGLRTR
LLVTALVGAG LGGAWLALRA EKERGRQQQR TEALRQAAVG QGDFSLLDHR GRVRCKADFR
GQWVLLYFGF THCPDICPDE LEKLVQVVRQ LEAEPGLPPV QPLFITVDPE RDTVAAMARY
VQDFHPRLLG LTGSAEQIAQ VSRSYRVYYS AGPKDEDQDY IVDHSIAIYL LSPDGLFTDY
YSRARSAEQI TDSVRRHMAA FRSVLR
